PMID:11053866
| Citation |
Borek, D and Jaskólski, M (2000) Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome. Acta Crystallogr. D Biol. Crystallogr. 56:1505-7 |
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| Abstract |
A new Escherichia coli L-asparaginase belonging to the class of Ntn amidohydrolases has been crystallized using the vapour-diffusion method and PEG 4000 as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) (unit-cell parameters a = 50. 3, b = 77.6, c = 148.2 A) and diffract to 1.65 A resolution. The structure has been solved by molecular replacement using aspartylglucosaminidase from Flavobacterium meningosepticum as the search model. The asymmetric unit contains four protein chains composed into a dimer of alphabeta heterodimers, where the subunits alpha and beta are the product of autoproteolytic cleavage of the immature protein. |
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| Keywords |
Amino Acid Sequence; Asparaginase/chemistry; Asparaginase/genetics; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Genome, Bacterial; Humans; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid |
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